Calcium in PDB 3zm8: Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase

Enzymatic activity of Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase

All present enzymatic activity of Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase:
3.2.1.78;

Protein crystallography data

The structure of Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase, PDB code: 3zm8 was solved by M.Couturier, A.Roussel, A.Rosengren, P.Leone, H.Stalbrand, J.G.Berrin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.30 / 2.85
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 97.490, 97.490, 268.717, 90.00, 90.00, 120.00
R / Rfree (%) 20.63 / 25.73

Other elements in 3zm8:

The structure of Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase (pdb code 3zm8). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase, PDB code: 3zm8:

Calcium binding site 1 out of 1 in 3zm8

Go back to Calcium Binding Sites List in 3zm8
Calcium binding site 1 out of 1 in the Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Podospora Anserina GH26-CBM35 Beta-(1,4)-Mannanase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1450

b:90.4
occ:1.00
O A:GLY35 2.3 96.0 1.0
OE1 A:GLU13 2.3 85.5 1.0
OD1 A:ASP123 2.3 74.8 1.0
OE1 A:GLU15 2.4 79.2 1.0
O A:THR32 2.6 87.8 1.0
O A:ASP123 2.8 78.3 1.0
OE2 A:GLU15 2.9 86.0 1.0
CD A:GLU15 3.0 94.2 1.0
C A:GLY35 3.3 95.9 1.0
CD A:GLU13 3.5 79.6 1.0
C A:ASP123 3.5 78.4 1.0
CG A:ASP123 3.5 77.2 1.0
C A:THR32 3.7 88.5 1.0
CA A:ASP123 3.8 74.3 1.0
N A:TYR36 4.1 92.6 1.0
N A:GLY35 4.1 90.8 1.0
CB A:GLU13 4.2 65.0 1.0
CB A:ASP123 4.2 75.2 1.0
CG A:GLU13 4.2 66.2 1.0
CA A:TYR36 4.2 92.2 1.0
OG1 A:THR32 4.3 87.8 1.0
N A:THR32 4.3 88.8 1.0
CA A:GLY35 4.3 91.0 1.0
N A:ALA14 4.4 67.8 1.0
OE2 A:GLU13 4.4 61.0 1.0
CG A:GLU15 4.5 80.4 1.0
OD2 A:ASP123 4.5 82.9 1.0
CA A:THR32 4.5 86.9 1.0
CA A:GLU13 4.6 64.6 1.0
N A:SER124 4.6 74.1 1.0
N A:GLY33 4.6 83.7 1.0
CB A:TYR31 4.7 94.9 1.0
CA A:GLY33 4.7 83.2 1.0
CB A:TYR36 4.8 93.7 1.0
N A:ARG34 4.9 86.0 1.0
C A:GLU13 4.9 70.5 1.0
CD1 A:TYR31 4.9 98.9 1.0
CB A:SER124 4.9 74.7 1.0
N A:GLU15 4.9 72.8 1.0
C A:GLY33 5.0 87.5 1.0

Reference:

M.Couturier, A.Roussel, A.Rosengren, P.Leone, H.Stalbrand, J.G.Berrin. Structural and Biochemical Analyses of Glycoside Hydrolase Families 5 and 26 Beta-(1,4)-Mannanases From Podospora Anserina Reveal Differences Upon Manno-Oligosaccharides Catalysis. J.Biol.Chem. V. 288 14624 2013.
ISSN: ISSN 0021-9258
PubMed: 23558681
DOI: 10.1074/JBC.M113.459438
Page generated: Sat Dec 12 04:37:18 2020

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